5MUS
Structure of the C-terminal domain of a reptarenavirus L protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-07 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 76.392, 76.942, 116.920 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 63.950 - 2.009 |
| R-factor | 0.1999 |
| Rwork | 0.198 |
| R-free | 0.24210 |
| Structure solution method | SAD |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.927 |
| Data reduction software | iMOSFLM (7.1.3) |
| Data scaling software | SCALA |
| Phasing software | AutoSol |
| Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 63.950 | 2.081 |
| High resolution limit [Å] | 2.009 | 2.009 |
| Rmerge | 0.050 | |
| Rmeas | 0.070 | |
| Number of reflections | 45942 | 4525 |
| <I/σ(I)> | 8.36 | 1.51 |
| Completeness [%] | 98.0 | 99 |
| Redundancy | 1.9 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 37% Jeffamine ED-2001, 2 mM TCEP and 100 mM HEPES pH 7.1 |
